Deactivating Chemical Agents Using Enzyme-Coated Nanofibers Formed by Electrospinning
Source abstract
Abstract
The coaxial electrospinning technique was investigated as a novel method to create stabilized, enzyme-containing fibers that have the potential to provide enhanced protection from chemical agents. Electrospinning is a versatile technique for the fabrication of polymer fibers with large length (cm to km): diameter (nm to μm) aspect ratios. The large surface to volume ratios, along with the biofriendly nature of this technique, enables the fabrication of fiber mats with high enzyme concentrations, which amplify the catalytic activity per unit volume of membrane. Blended composite (single-source) fibers incorporate enzyme throughout the fiber, which may limit substrate accessibility to the enzyme. In contrast, core/sheath fibers can be produced by coaxial electrospinning with very high enzyme loading (>80%) in the sheath without noticeable loss of enzymatic activity. Several core-sheath combinations have been explored with the toxin-mitigating enzyme DFPase in order to achieve fibers with optimum properties. The concentration of fluoride released, normalized for the amount of protein incorporated into the sheath, was used as a measure of the enzyme activity versus time. The coaxial core/sheath combination of PEO and DFPase produced the highest activity (~7.3 mM/mg).
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Electrospun Nanofibers in Biomedical Applications · Electrochemical sensors and biosensors · Graphene and Nanomaterials Applications
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Nanoelectronics Laboratory, University of Cincinnati, Cincinnati, Ohio 45221-0030, United States
Biological Science and Technology Team (BSTT), Natick Soldier Research Development and Engineering Center, Natick, Massachusetts, United States
References (32)
Show source-provided references
1. Hoskin F. C. G. · Science · 1971 · 172 · 124310.1126/science.172.3989.1243 ↗
2. Hoskin F. C. · Science · 1982 · 215 · 125510.1126/science.7058344 ↗
3. Rogers J. · 2009
4. Richardt A. · 200810.1002/9783527621620 ↗
5. Hartleib J. · Protein Expression Purif. · 2001 · 21 · 21010.1006/prep.2000.1360 ↗
6. Blum M.-M.. · J. Am. Chem. Soc. · 2007 · 128 · 1275010.1021/ja061887n ↗
7. Katesmi V. · Biochemistry · 2005 · 44 · 902210.1021/bi0500675 ↗
8. Krajewska B. · Enzyme Microb. Technol. · 2004 · 35 · 12610.1016/j.enzmictec.2003.12.013 ↗
9. Lee K. · Fibers and Polymers · 2005 · 6 · 18110.1007/BF02875641 ↗
10. Pal A. · Process Biochem. · 2011 · 46 · 131510.1016/j.procbio.2011.02.024 ↗
11. Herricks T. E. · J. Mater. Chem. · 2005 · 15 · 324110.1039/b503660g ↗
12. Wang Z.-G. · J. Mol. Catal. B: Enzym. · 2009 · 56 · 18910.1016/j.molcatb.2008.05.005 ↗
13. Jia H. · Biotechnol. Prog. · 2002 · 18 · 102710.1021/bp020042m ↗
14. Wang Y. · J. Membr. Sci. · 2008 · 309 · 7310.1016/j.memsci.2007.10.008 ↗
15. Ye P. · Macromolecules · 2005 · 39 · 104110.1021/ma0517998 ↗
16. Ye P. · Biomaterials · 2006 · 27 · 416910.1016/j.biomaterials.2006.03.027 ↗
17. Hwang E. T. · J. Mater. Chem. · 2011 · 21 · 521510.1039/c0jm02969f ↗
18. Kim T. G. · Biotechnol. Prog. · 2006 · 22 · 110810.1021/bp060039t ↗
19. Drevon G. F. · Biomacromolecules · 2000 · 1 · 57110.1021/bm0000034 ↗
20. Drevon G. F. · Biotechnol. Bioeng. · 2002 · 79 · 78510.1002/bit.10334 ↗
21. Filocamo S. · J. Mater. Res. · 2011 · 26 · 104210.1557/jmr.2011.33 ↗
22. Kim J. · Chem. Eng. Sci. · 2006 · 61 · 101710.1016/j.ces.2005.05.067 ↗
23. Cao L. · Org. Lett. · 2000 · 2 · 136110.1021/ol005593x ↗
24. Kim B. C. · Nanotechnology · 2005 · 16 · S38210.1088/0957-4484/16/7/011 ↗
25. Wang Y. · J. Polym. Sci., Part A: Polym. Chem. · 2004 · 42 · 428910.1002/pola.20271 ↗
26. Xie J. · J. Mater. Sci. · 2003 · 38 · 212510.1023/A:1023763727747 ↗
27. Jiang H. · J. Controlled Release · 2005 · 108 · 23710.1016/j.jconrel.2005.08.006 ↗
28. Han D. · Mater. Res. Soc. Symp. Proc. · 2008 · 1094 · 1094
29. Han D. · Langmuir · 2009 · 25 · 945410.1021/la900660v ↗
30. Bedford N. M. · ACS Appl. Mater. Interfaces · 2010 · 2 · 244810.1021/am1005089 ↗
31. Hoskin F. C. G. · Chem.-Biol. Interact. · 1999 · 119 · 43910.1016/S0009-2797(99)00056-3 ↗
32. Hartleib J. · Biochim. Biophys. Acta, Protein Struct. Mol. Enzymol. · 2001 · 1546 · 31210.1016/S0167-4838(01)00153-4 ↗